Immobilized β-d-galactosidases for improved synthesis of short chain galactooligosaccharides

Anamaria Todea, C.G. Boeriu, Francisc Peter, Emese Biro

Research output: Chapter in Book/Report/Conference proceedingChapterAcademic

Abstract

As much as digesting of lactose emerged as an important health and nutritional problem and the deficiency of this hydrolytic enzyme showed increasing tendency, the consumption of lactose-free beverages became a possible solution for people owing lactose intolerance. Therefore, β-d-galactosidase (β-GAL), the enzyme responsible for lactose hydrolysis to glucose and galactose, has achieved wide utilization in the food technology, mainly in the dairy industry. In the same time, β-GAL is able to catalyze the transgalactosylation reaction leading to galacto-oligosaccharides (GOS). GOS belong to the group of nondigestible prebiotics that beneficially affect the organisms by stimulating the growth and activity of useful bacteria in the colon, reducing the gastrointestinal discomfort. GOS fortified foods and beverages have an important and increasing market potential in all age groups, but particularly in infant population. The GOS market is already consolidated, but technological improvements are always needed. Immobilization of enzymes is a well-known method to improve the stability and confer reusability of the enzymes, particularly in large-scale applications. The utilization of immobilized β-GAL for lactose hydrolysis was subject of numerous studies, while GOS synthesis with the same biocatalyst involves specific requirements, particularly when continuous processes are targeted. This review presents the recent advancements in the topic of β-GAL immobilization by various methods and a comparative overview on the main approaches concerning the synthesis of short-chain GOS using the immobilized biocatalyst, with possible applications in the beverage industry.
Original languageEnglish
Title of host publicationBiotechnological progress and Beverage Consumption
Chapter3
Pages71-110
Volume19
DOIs
Publication statusPublished - 2019

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